In a viral infection model, the administration of Guanidine hydrochloride at a dose of 145 mg/kg per injection given twice to infant mice infected with ten LD50 of coxsackievirus A16, 58 hours post-infection, significantly reduces mortality rates^[4].

At low concentrations, it refolds acid-unfolded apomyoglobin and cytochrome c, stabilizing the molten globule state. This state is characterized by a compact but denatured structure with considerable secondary structure yet significantly disordered tertiary structure. Conversely, at concentrations greater than 1 M, Guanidine hydrochloride induces a cooperative unfolding of this molten globule state^[1].

At millimolar concentrations, Guanidine hydrochloride effectively eliminates the normally stable [PSI+] prion element from yeast cells. Specifically, 5 mM of Guanidine hydrochloride in the growth media not only cures [PSI+] but also other yeast prions. Additionally, this concentration substantially diminishes the heat shock protein Hsp104-mediated basal and acquired thermotolerance by 30-fold and 50-fold, respectively, and also reduces Hsp104’s ability to reactivate thermally denatured luciferase^[3].